Mass Spectrometry Reviews最新文献

{"title":"The Rise of Top-Down Mass Spectrometry for the Characterization of Oligonucleotide Therapeutics","authors":"Molly S. Blevins,&nbsp;Christopher M. Crittenden,&nbsp;Bifan Chen","doi":"10.1002/mas.70037","DOIUrl":"10.1002/mas.70037","url":null,"abstract":"<div>\u0000 \u0000 <p>The therapeutic landscape has been rapidly expanding beyond traditional small molecules and biologics in recent years with the emergence of oligonucleotide therapeutics. As these oligonucleotide modalities grow in complexity and chemical modifications, conventional digestion-based mass spectrometry strategies start to yield redundant and ambiguous information. Alternatively, the top-down approach has the potential to provide a holistic view of therapeutic oligonucleotides. This review examines the rise of top-down mass spectrometry for the characterization of therapeutic oligonucleotides, with a focus on technological and methodological advances between 2020 and 2025. We cover sample preparation, sample introduction including separation, ionization, mass analysis, fragmentation approaches, data analysis strategies, and a discussion of long oligonucleotide and beyond for oligonucleotide top-down analysis. Finally, we provide a practical top-down workflow guidance on therapeutic oligonucleotides and conclude with a forward-looking perspective on the frontiers of the field.</p></div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 6","pages":"1117-1139"},"PeriodicalIF":6.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148409809","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The TriVersa NanoMate: Automation of Nano Electrospray Analyses","authors":"Simon Prosser,&nbsp;Gary Schultz,&nbsp;Thomas Corso,&nbsp;Daniel Eikel,&nbsp;Thomas Kurz,&nbsp;Jamey Jones,&nbsp;Jack Henion","doi":"10.1002/mas.70021","DOIUrl":"10.1002/mas.70021","url":null,"abstract":"<div>\u0000 \u0000 <p>The evolution of nano-electrospray ionization technology began in the mid-1980s. At that time, no commercial vendors supplied the requisite electrospray emitters, which featured internal diameters of just a few microns. Tips were manually fabricated by pulling heated glass capillaries to create micron and sub-micron inside diameter tips. High voltage was applied to a sample solution within the capillary body, and when placed close to a counter electrode of the atmospheric pressure ionization (API) mass spectrometer formed a sufficiently high electric field to produce an electrospray plume. Nano electrospray offered key advantages, including enhanced sensitivity and minimized matrix effects for chemical analysis due to better ionization efficiency and reduced contamination due to the lower mass transfer into the mass spectrometer orifice. By the late 1990s, Advion scientists utilized the Cornell Nanofabrication Facility equipment to create an array of nano-electrospray emitters etched in a silicon wafer. Key to the success of this planar emitter array was the inclusion of a dielectric layer that enabled the formation of an electric field estimated to be equivalent to that of a pulled glass capillary emitter with dimensions near one micron, but with a 28 micron outside diameter emitter. This “ESI Chip” was commercialized along with a robot named NanoMate to enable automated, reproducible, and robust nano electrospray of 96 consecutive samples from the chip-based array of micro-fabricated emitters. This paper explores the development and commercialization story of the NanoMate and its use to expand scientific knowledge in the field of protein non-covalent interactions, protein structure, lipidomics, drug metabolism, and a host of other applications.</p>\u0000 </div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 6","pages":"1028-1039"},"PeriodicalIF":6.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146256891","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Development of the Digital Ion Trap","authors":"Li Ding,&nbsp;Lulu Sun,&nbsp;Weimin Wang","doi":"10.1002/mas.70022","DOIUrl":"10.1002/mas.70022","url":null,"abstract":"<div>\u0000 \u0000 <p>The digital ion trap (DIT) is an ion trap in which the periodic trapping field is driven by digital signals—typically with a rectangular waveform—generated by fast-switching circuits. This paper reviews the research history of rectangular wave-driven quadrupole fields, as well as the invention and development of DITs. It summarizes studies on ion motion stability and secular frequency in both 3D and 2D configurations of DITs and discusses differences in the stability diagrams of DITs arising from different definitions of the <i>a</i> and <i>q</i> parameters. Additionally, this review outlines the performance advantages of the digital driving method in mass analysis and lists the novel analytical functions that have been realized using DIT technology. Finally, it presents the latest developments in commercial DIT instruments.</p>\u0000 </div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 6","pages":"1040-1063"},"PeriodicalIF":6.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147483966","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Rise of Trapped Ion Mobility Spectrometry: Principles, Applications, and Recent Developments","authors":"Erin M. Panczyk,&nbsp;Claudia Martelli,&nbsp;Mark E. Ridgeway,&nbsp;Mans Ekeloef,&nbsp;Daniel Hornburg,&nbsp;Benjamin J. Jones,&nbsp;Christopher A. Wootton,&nbsp;Matthew R. Lewis,&nbsp;Stuart Pengelley,&nbsp;Jean-Francois Greisch,&nbsp;Melvin A. Park","doi":"10.1002/mas.70034","DOIUrl":"10.1002/mas.70034","url":null,"abstract":"<div>\u0000 \u0000 <p>Trapped ion mobility spectrometry (TIMS) is a highly versatile alternative to the more conventional drift tube ion mobility spectrometer (DTIMS). In TIMS, ions are analyzed using an electric field that holds ions stationary against moving gas. In the basic TIMS, ions are accumulated and trapped in the electric field and then eluted over time according to their collision cross section (CCS) as the strength of the electric field is scanned down. The resultant small size and low operating voltage of TIMS compared to prior approaches make it ideal for hybridization with mass spectrometry. Since its introduction and coupling with Time-of-Flight Mass Spectrometry (TOFMS) in 2011, TIMS has been widely and successfully applied in various bioanalytical fields, including proteomics, glycomics, metabolomics, lipidomics, and native mass spectrometry. In particular, the first commercial TIMS-MS instrument introduced by Bruker Daltonics Inc. (timsTOF), launched in 2016, quickly shined as one of the main reference instruments in bottom-up proteomics. The increased peak capacity, resulting from the additional dimension of separation—that is, mobility—leads to mass spectra of reduced complexity and a greater depth of peptide identification. In this retrospective, different designs and operational modes of TIMS will be presented with a focus on the advantages, potentials and challenges of this technology within the fields of the omics sciences, spanning from metabolomics to structural biology, including single cell analysis. Additionally, the newest platforms utilizing TIMS technology will be introduced, with a focus on future applications and direction of the technology.</p>\u0000 </div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 6","pages":"1087-1116"},"PeriodicalIF":6.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148262437","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"First 20 Years of Orbitrap Mass Spectrometry as the Mainstream Analytical Technique","authors":"Alexander Makarov","doi":"10.1002/mas.70024","DOIUrl":"10.1002/mas.70024","url":null,"abstract":"<p>This review traces the first 20 years of Orbitrap mass spectrometry as a mainstream high‑resolution and accurate‑mass (HR/AM) technology. It outlines the historical development of the Orbitrap analyzer, the evolution of major instrument families, and the key technological innovations that enabled its widespread adoption. Particular emphasis is placed on hybrid and Tribrid architectures, democratization of HR/AM through benchtop platforms, extension to high‑mass and native analysis, and integration with ion mobility, advanced fragmentation methods, and emerging applications such as structural biology, isotope ratio measurements, and space research. The review concludes with a perspective on future directions and the anticipated role of Orbitrap instrumentation as the core workhorse in analytical laboratories worldwide.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 6","pages":"1064-1086"},"PeriodicalIF":6.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/mas.70024","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147632058","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Focus Issue: Mass Spectrometry in Industry","authors":"Richard B. Cole","doi":"10.1002/mas.70044","DOIUrl":"10.1002/mas.70044","url":null,"abstract":"","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 6","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148962860","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Analysis of Carbohydrates and Glycoconjugates by Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry: An Update for 2023-2024.","authors":"David J Harvey","doi":"10.1002/mas.70029","DOIUrl":"https://doi.org/10.1002/mas.70029","url":null,"abstract":"<p><p>The use of MALDI mass spectrometry for the analysis of carbohydrates and glycoconjugates is a well-established technique and this comprehensive review is the twelfth update of the original article published in 1999 and brings coverage of the literature to the end of 2024. Although still popular for glycoconjugate analysis, recent years have seen a slight drop in its usage with electrospray and LC-MS techniques becoming more widely used. The review follows the same general format as previous reviews. Much of the material relating to applications is presented in tabular form whereas papers relating to method development are discussed in more detail. The review is divided into three sections: (1) general aspects such as theory of the MALDI process, matrices, derivatization, MALDI imaging, fragmentation, quantification, and the use of computer software for structural identification. (2) Applications to various structural types such as oligo- and polysaccharides, glycoproteins, glycated proteins, glycolipids and natural products, and (3) other general areas such as medicine, biopharmaceuticals, industrial processes and glycan synthesis where MALDI is extensively used. As with previous reviews in this series, this review also includes a few papers that describe methods appropriate to analysis by MALDI, such as sample preparation, even though the ionization method is not MALDI. Much of this work is tabulated. MALDI is still an ideal technique for carbohydrate analysis, particularly in its rapidity, ease of use and its ability to produce single ions from each analyte. Improvements in the technique and range of applications show little sign of diminishing.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149035805","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mass Spectrometry in Authentication and Forensic Approaches for Determining the Origin of Hazardous Chemicals.","authors":"Carla Orlandi, Grégoire Delaporte, Christine Albaret, Emmanuel Joubert, Anne Bossée, Emilien L Jamin, Laurent Debrauwer","doi":"10.1002/mas.70043","DOIUrl":"https://doi.org/10.1002/mas.70043","url":null,"abstract":"<p><p>Identification of a chemical agent yields insights into its physicochemical properties. By examining the intrinsic characteristics and environment of a compound, information about its history can be gathered. The main objective of authentication/forensic approaches to chemicals is to trace the history of the compound's origin, regardless of its nature (e.g., environmental pollutants, drugs, or toxicants). This review presents several scientific fields that share a common objective: using mass spectrometry (MS) to obtain source information from diverse samples and chemicals. From targeted analysis to the full screening of non-targeted chemical space, direct and coupled MS approaches provide powerful capabilities for addressing source-determination concerns, as described in this review. Novel sampling and ionization methods have proven to have a significant impact on expanding MS applications across diverse sample types. This review covers the main methods for determining chemical origins, ranging from targeted confirmation of known compounds to non-targeted identification of unknown compounds under challenging experimental and matrix-related conditions.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-09-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148899914","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Proteoforms in Disease: Biomedical Applications of Top-Down Proteomics.","authors":"Holden T Rogers, Zachery R Gregorich, Megan S Gant, Zhan Gao, Julia Chamot-Rooke, Ying Ge","doi":"10.1002/mas.70042","DOIUrl":"10.1002/mas.70042","url":null,"abstract":"<p><p>The proteome is a dynamic landscape of proteoforms arising from genetic mutations, alternative splicing, and post-translational modifications (PTMs), which collectively drive biological function and disease phenotypes. Mass spectrometry (MS)-based proteomics has emerged as an essential technique for elucidating this molecular complexity. Although bottom-up proteomics enables deep protein identification and quantification through peptide-level analysis, it disrupts molecular connectivity and introduces a peptide-to-protein inference problem, which is suboptimal for proteoform analysis. Top-down proteomics (TDP) offers a complementary approach by analyzing intact proteins, preserving molecular connectivity, and enabling direct characterization and quantification of proteoforms. This capability is increasingly vital for understanding heterogeneous human diseases. Here, we review the evolving role of TDP in biomedical research, highlighting studies that revealed proteoform-level alterations, identified candidate biomarkers, and advanced our understanding of the roles of proteoforms in human diseases.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890486","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Advances in Mass Spectrometry-Based Proteomics for Kidney Disease Biomarker Discovery and Clinical Translation.","authors":"Yingying Ling, Fei Cai, Ling Li, Yonghong Mao, Guisen Li, Xinfang Xie, Zhenyu Sun, Rajeev K Singla, Shuyun Liu, Wanjun Zhao, Yong Zhang","doi":"10.1002/mas.70041","DOIUrl":"https://doi.org/10.1002/mas.70041","url":null,"abstract":"<p><p>The high prevalence and substantial burden of kidney diseases necessitate advanced approaches to elucidate molecular mechanisms and promote precision medicine. Mass spectrometry (MS)-based proteomics has evolved into a widely used analytical platform, delivering high-sensitivity, high-throughput protein profiling capabilities that have contributed substantially to biomarker discovery, mechanistic dissection, and therapeutic target identification across a broad range of kidney diseases. This review provides a comprehensive overview of MS-based proteomics applications in kidney disease research, covering progress in biomarker identification, pathogenic mechanism interrogation, and clinical translation. It highlights methodological advances, emerging trends, and persistent challenges that shape the field. Existing literature has uncovered abundant disease-specific biomarkers and revealed key pathogenic pathways, including podocyte injury-associated protein interaction networks, dysregulated complement activation, and metabolic reprogramming, and have critically assessed their translational potential. Additionally, investigations into posttranslational modifications such as phosphorylation and glycosylation have provided valuable insights for targeted therapies. Collectively, these findings illustrate the contributions of MS-based proteomics to the characterization of disease molecular heterogeneity, the identification of key pathogenic drivers, and the development of precision medicine approaches. This review further addresses current challenges in clinical applications, including sample heterogeneity, data complexity, and standardization issues. We additionally emphasize the critical need for minimum reporting standards and multicenter harmonization to accelerate the clinical translation of renal proteomics. Future research should focus on integrating multiomics and artificial intelligence-driven data mining to enhance precise disease subtyping, dynamic monitoring, and personalized treatment strategies.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786215","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}